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{{Infobox_gene}}
'''DNA repair protein REV1''' is a [[protein]] that in humans is encoded by the ''REV1'' [[gene]].<ref name="pmid10536157">{{cite journal |vauthors=Lin W, Xin H, Zhang Y, Wu X, Yuan F, Wang Z | title = The human REV1 gene codes for a DNA template-dependent dCMP transferase | journal = Nucleic Acids Res | volume = 27 | issue = 22 | pages = 4468–75 |date=Dec 1999 | pmid = 10536157 | pmc = 148731 | doi =10.1093/nar/27.22.4468  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: REV1 REV1 homolog (S. cerevisiae)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51455| accessdate = }}</ref> <!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein with similarity to the [[S. cerevisiae]] [[mutagenesis]] protein Rev1. The Rev1 proteins contain a [[BRCT domain]], which is important in [[protein-protein interactions]]. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA [[polymerase]]s involved in [[translesion synthesis]] (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.<ref name="entrez"/>
}} Rev1 is a [[DNA polymerase#Family Y|Y family DNA polymerase]]; it is sometimes referred to as a ''deoxycytidyl transferase'' because it only inserts [[deoxycytidine]] (dC) across from lesions. Whether [[Guanine|G]], [[Adenine|A]], [[Thymine|T]], [[Cytidine|C]], or an [[AP site|abasic site]], Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an [[arginine]] as a template which complements well with C.<ref>{{Cite journal|title = Rev1 employs a novel mechanism of DNA synthesis using a protein template|last = Nair|first = DT|date = Sep 30, 2005|journal = Science|doi = 10.1126/science.1116336|pmid = 16195463|volume=309|pages=2219–22}}</ref> Yet it is believed{{By whom|date=May 2011}} that Rev1 rarely uses its polymerase activity; rather it is thought that Rev1's primary role is as a protein landing pad, whereby it helps direct the recruitment of TLS proteins, especially Pol ζ ([[REV3L|Rev3]]/Rev7).
==Interactions==
REV1 has been shown to [[Protein-protein interaction|interact]] with [[MAD2L2]].<ref name=pmid11485998>{{cite journal |last=Murakumo |first=Y |authorlink= |author2=Ogura Y |author3=Ishii H |author4=Numata S |author5=Ichihara M |author6=Croce C M |author7=Fishel R |author8=Takahashi M  |date=September 2001 |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7 |journal=J. Biol. Chem. |volume=276 |issue=38 |pages=35644–51 |publisher= |location = United States| issn = 0021-9258| pmid = 11485998 |doi = 10.1074/jbc.M102051200 | bibcode = | oclc =| id = | url = | language = | laysummary = | laysource = | laydate = | quote = }}</ref> It is believed that Rev1 may interact with PCNA, once [[ubiquitylated]] due to a lesion, and help recruit Pol ζ ([[REV3L|Rev3]]/Rev7) a B family polymerase involved in TLS.
==References==
{{Reflist}}
==Further reading==
{{Refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  |vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791  }}
*{{cite journal  |vauthors=Wixler V, Laplantine E, Geerts D, etal |title=Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains. |journal=FEBS Lett. |volume=445 |issue= 2-3 |pages= 351–5 |year= 1999 |pmid= 10094488 |doi=10.1016/S0014-5793(99)00151-9  }}
*{{cite journal  |vauthors=Gibbs PE, Wang XD, Li Z, etal |title=The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4186–91 |year= 2000 |pmid= 10760286 |doi=10.1073/pnas.97.8.4186  | pmc=18191  }}
*{{cite journal  |vauthors=Wixler V, Geerts D, Laplantine E, etal |title=The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33669–78 |year= 2000 |pmid= 10906324 |doi= 10.1074/jbc.M002519200 }}
*{{cite journal  |vauthors=Masuda Y, Takahashi M, Tsunekuni N, etal |title=Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15051–8 |year= 2001 |pmid= 11278384 |doi= 10.1074/jbc.M008082200 }}
*{{cite journal  |vauthors=Murakumo Y, Ogura Y, Ishii H, etal |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35644–51 |year= 2001 |pmid= 11485998 |doi= 10.1074/jbc.M102051200 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  |vauthors=Masuda Y, Ohmae M, Masuda K, Kamiya K |title=Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. |journal=J. Biol. Chem. |volume=278 |issue= 14 |pages= 12356–60 |year= 2003 |pmid= 12529368 |doi= 10.1074/jbc.M211765200 }}
*{{cite journal  |vauthors=Clark DR, Zacharias W, Panaitescu L, McGregor WG |title=Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene. |journal=Nucleic Acids Res. |volume=31 |issue= 17 |pages= 4981–8 |year= 2004 |pmid= 12930947 |doi=10.1093/nar/gkg725  | pmc=212819  }}
*{{cite journal  |vauthors=Guo C, Fischhaber PL, Luk-Paszyc MJ, etal |title=Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6621–30 |year= 2004 |pmid= 14657033 |doi= 10.1093/emboj/cdg626  | pmc=291821 }}
*{{cite journal  |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Ohashi E, Murakumo Y, Kanjo N, etal |title=Interaction of hREV1 with three human Y-family DNA polymerases. |journal=Genes Cells |volume=9 |issue= 6 |pages= 523–31 |year= 2005 |pmid= 15189446 |doi= 10.1111/j.1356-9597.2004.00747.x }}
*{{cite journal  |vauthors=Tissier A, Kannouche P, Reck MP, etal |title=Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein. |journal=DNA Repair (Amst.) |volume=3 |issue= 11 |pages= 1503–14 |year= 2005 |pmid= 15380106 |doi= 10.1016/j.dnarep.2004.06.015 }}
*{{cite journal  |vauthors=Hillier LW, Graves TA, Fulton RS, etal |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724–31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 }}
*{{cite journal  |vauthors=Lin X, Okuda T, Trang J, Howell SB |title=Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells. |journal=Mol. Pharmacol. |volume=69 |issue= 5 |pages= 1748–54 |year= 2006 |pmid= 16495473 |doi= 10.1124/mol.105.020446 }}
*{{cite journal  |vauthors=Masuda Y, Kamiya K |title=Role of single-stranded DNA in targeting REV1 to primer termini. |journal=J. Biol. Chem. |volume=281 |issue= 34 |pages= 24314–21 |year= 2006 |pmid= 16803901 |doi= 10.1074/jbc.M602967200 }}
*{{cite journal  |vauthors=Yuasa MS, Masutani C, Hirano A, etal |title=A human DNA polymerase eta complex containing Rad18, Rad6 and Rev1; proteomic analysis and targeting of the complex to the chromatin-bound fraction of cells undergoing replication fork arrest. |journal=Genes Cells |volume=11 |issue= 7 |pages= 731–44 |year= 2006 |pmid= 16824193 |doi= 10.1111/j.1365-2443.2006.00974.x }}
}}
{{Refend}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = REV1 homolog (S. cerevisiae)
| HGNCid = 14060
| Symbol = REV1
| AltSymbols =; FLJ21523; MGC163283; MGC26225; REV1L
| OMIM = 606134
| ECnumber = 
| Homologene = 32309
| MGIid = 1929074
| GeneAtlas_image1 = PBB_GE_REV1_218428_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0017125 |text = deoxycytidyl transferase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006280 |text = mutagenesis}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0009411 |text = response to UV}} {{GNF_GO|id=GO:0042276 |text = error-prone postreplication DNA repair}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 51455
    | Hs_Ensembl = ENSG00000135945
    | Hs_RefseqProtein = NP_001032961
    | Hs_RefseqmRNA = NM_001037872
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 99383846
    | Hs_GenLoc_end = 99472912
    | Hs_Uniprot = Q9UBZ9
    | Mm_EntrezGene = 56210
    | Mm_Ensembl = ENSMUSG00000026082
    | Mm_RefseqmRNA = NM_019570
    | Mm_RefseqProtein = NP_062516
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 37997330
    | Mm_GenLoc_end = 38074208
    | Mm_Uniprot = Q3V4D4
  }}
}}
'''REV1 homolog (S. cerevisiae)''', also known as '''REV1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: REV1 REV1 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51455| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a protein with similarity to the S. cerevisiae mutagenesis protein Rev1. The Rev1 proteins contain a BRCT domain, which is important in protein-protein interactions. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.<ref name="entrez">{{cite web | title = Entrez Gene: REV1 REV1 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=51455| accessdate = }}</ref>
}}
==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | author=Wixler V, Laplantine E, Geerts D, ''et al.'' |title=Identification of novel interaction partners for the conserved membrane proximal region of alpha-integrin cytoplasmic domains. |journal=FEBS Lett. |volume=445 |issue= 2-3 |pages= 351-5 |year= 1999 |pmid= 10094488 |doi=  }}
*{{cite journal  | author=Lin W, Xin H, Zhang Y, ''et al.'' |title=The human REV1 gene codes for a DNA template-dependent dCMP transferase. |journal=Nucleic Acids Res. |volume=27 |issue= 22 |pages= 4468-75 |year= 1999 |pmid= 10536157 |doi=  }}
*{{cite journal  | author=Gibbs PE, Wang XD, Li Z, ''et al.'' |title=The function of the human homolog of Saccharomyces cerevisiae REV1 is required for mutagenesis induced by UV light. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 8 |pages= 4186-91 |year= 2000 |pmid= 10760286 |doi=  }}
*{{cite journal  | author=Wixler V, Geerts D, Laplantine E, ''et al.'' |title=The LIM-only protein DRAL/FHL2 binds to the cytoplasmic domain of several alpha and beta integrin chains and is recruited to adhesion complexes. |journal=J. Biol. Chem. |volume=275 |issue= 43 |pages= 33669-78 |year= 2000 |pmid= 10906324 |doi= 10.1074/jbc.M002519200 }}
*{{cite journal  | author=Masuda Y, Takahashi M, Tsunekuni N, ''et al.'' |title=Deoxycytidyl transferase activity of the human REV1 protein is closely associated with the conserved polymerase domain. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 15051-8 |year= 2001 |pmid= 11278384 |doi= 10.1074/jbc.M008082200 }}
*{{cite journal  | author=Murakumo Y, Ogura Y, Ishii H, ''et al.'' |title=Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7. |journal=J. Biol. Chem. |volume=276 |issue= 38 |pages= 35644-51 |year= 2001 |pmid= 11485998 |doi= 10.1074/jbc.M102051200 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Masuda Y, Ohmae M, Masuda K, Kamiya K |title=Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins. |journal=J. Biol. Chem. |volume=278 |issue= 14 |pages= 12356-60 |year= 2003 |pmid= 12529368 |doi= 10.1074/jbc.M211765200 }}
*{{cite journal  | author=Clark DR, Zacharias W, Panaitescu L, McGregor WG |title=Ribozyme-mediated REV1 inhibition reduces the frequency of UV-induced mutations in the human HPRT gene. |journal=Nucleic Acids Res. |volume=31 |issue= 17 |pages= 4981-8 |year= 2004 |pmid= 12930947 |doi=  }}
*{{cite journal  | author=Guo C, Fischhaber PL, Luk-Paszyc MJ, ''et al.'' |title=Mouse Rev1 protein interacts with multiple DNA polymerases involved in translesion DNA synthesis. |journal=EMBO J. |volume=22 |issue= 24 |pages= 6621-30 |year= 2004 |pmid= 14657033 |doi= 10.1093/emboj/cdg626 }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Ohashi E, Murakumo Y, Kanjo N, ''et al.'' |title=Interaction of hREV1 with three human Y-family DNA polymerases. |journal=Genes Cells |volume=9 |issue= 6 |pages= 523-31 |year= 2005 |pmid= 15189446 |doi= 10.1111/j.1356-9597.2004.00747.x }}
*{{cite journal  | author=Tissier A, Kannouche P, Reck MP, ''et al.'' |title=Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein. |journal=DNA Repair (Amst.) |volume=3 |issue= 11 |pages= 1503-14 |year= 2005 |pmid= 15380106 |doi= 10.1016/j.dnarep.2004.06.015 }}
*{{cite journal  | author=Hillier LW, Graves TA, Fulton RS, ''et al.'' |title=Generation and annotation of the DNA sequences of human chromosomes 2 and 4. |journal=Nature |volume=434 |issue= 7034 |pages= 724-31 |year= 2005 |pmid= 15815621 |doi= 10.1038/nature03466 }}
*{{cite journal  | author=Lin X, Okuda T, Trang J, Howell SB |title=Human REV1 modulates the cytotoxicity and mutagenicity of cisplatin in human ovarian carcinoma cells. |journal=Mol. Pharmacol. |volume=69 |issue= 5 |pages= 1748-54 |year= 2006 |pmid= 16495473 |doi= 10.1124/mol.105.020446 }}
*{{cite journal  | author=Masuda Y, Kamiya K |title=Role of single-stranded DNA in targeting REV1 to primer termini. |journal=J. Biol. Chem. |volume=281 |issue= 34 |pages= 24314-21 |year= 2006 |pmid= 16803901 |doi= 10.1074/jbc.M602967200 }}
*{{cite journal  | author=Yuasa MS, Masutani C, Hirano A, ''et al.'' |title=A human DNA polymerase eta complex containing Rad18, Rad6 and Rev1; proteomic analysis and targeting of the complex to the chromatin-bound fraction of cells undergoing replication fork arrest. |journal=Genes Cells |volume=11 |issue= 7 |pages= 731-44 |year= 2006 |pmid= 16824193 |doi= 10.1111/j.1365-2443.2006.00974.x }}
}}
{{refend}}


{{protein-stub}}
{{Gene-2-stub}}
{{WikiDoc Sources}}

Revision as of 09:06, 10 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
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View/Edit Human

DNA repair protein REV1 is a protein that in humans is encoded by the REV1 gene.[1][2] This gene encodes a protein with similarity to the S. cerevisiae mutagenesis protein Rev1. The Rev1 proteins contain a BRCT domain, which is important in protein-protein interactions. A suggested role for the human Rev1-like protein is as a scaffold that recruits DNA polymerases involved in translesion synthesis (TLS) of damaged DNA. Two alternatively spliced transcript variants that encode different proteins have been found.[2] Rev1 is a Y family DNA polymerase; it is sometimes referred to as a deoxycytidyl transferase because it only inserts deoxycytidine (dC) across from lesions. Whether G, A, T, C, or an abasic site, Rev1 will always add a C. Rev1 has the ability to always add a C, because it uses an arginine as a template which complements well with C.[3] Yet it is believed[by whom?] that Rev1 rarely uses its polymerase activity; rather it is thought that Rev1's primary role is as a protein landing pad, whereby it helps direct the recruitment of TLS proteins, especially Pol ζ (Rev3/Rev7).

Interactions

REV1 has been shown to interact with MAD2L2.[4] It is believed that Rev1 may interact with PCNA, once ubiquitylated due to a lesion, and help recruit Pol ζ (Rev3/Rev7) a B family polymerase involved in TLS.

References

  1. Lin W, Xin H, Zhang Y, Wu X, Yuan F, Wang Z (Dec 1999). "The human REV1 gene codes for a DNA template-dependent dCMP transferase". Nucleic Acids Res. 27 (22): 4468–75. doi:10.1093/nar/27.22.4468. PMC 148731. PMID 10536157.
  2. 2.0 2.1 "Entrez Gene: REV1 REV1 homolog (S. cerevisiae)".
  3. Nair, DT (Sep 30, 2005). "Rev1 employs a novel mechanism of DNA synthesis using a protein template". Science. 309: 2219–22. doi:10.1126/science.1116336. PMID 16195463.
  4. Murakumo, Y; Ogura Y; Ishii H; Numata S; Ichihara M; Croce C M; Fishel R; Takahashi M (September 2001). "Interactions in the error-prone postreplication repair proteins hREV1, hREV3, and hREV7". J. Biol. Chem. United States. 276 (38): 35644–51. doi:10.1074/jbc.M102051200. ISSN 0021-9258. PMID 11485998.

Further reading